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P87228 (SERA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative D-3-phosphoglycerate dehydrogenase

Short name=3-PGDH
EC=1.1.1.95
Gene names
ORF Names:SPCC364.07, SPCC4G3.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH.

2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH.

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Serine biosynthesis
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processL-serine biosynthetic process

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

phosphoglycerate dehydrogenase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Putative D-3-phosphoglycerate dehydrogenase
PRO_0000076017

Regions

Nucleotide binding205 – 2062NAD By similarity
Nucleotide binding282 – 2843NAD By similarity
Nucleotide binding344 – 3474NAD By similarity

Sites

Active site2841 By similarity
Active site3131 By similarity
Active site3441Proton donor By similarity
Binding site2251NAD By similarity
Binding site3081NAD By similarity

Amino acid modifications

Modified residue871Phosphoserine Ref.2
Modified residue2581Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P87228 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 1E6EA04BF137C628

FASTA46650,883
        10         20         30         40         50         60 
MDIKGGRRGN VEDSLNKLSL SPPDNNSSFL SNHFQVRKSY SQAPARTLKP FASEDIKILL 

        70         80         90        100        110        120 
LENVNQSALS NLKDEGYQVE FLKTSMSEDD LVEKIKGVHA IGIRSKTRLT RRVLEAADSL 

       130        140        150        160        170        180 
IVIGCFCIGT NQVDLDFAAE RGIAVFNSPY ANSRSVAELV IGYIISLARQ VGDRSLELHR 

       190        200        210        220        230        240 
GEWNKVSSGC WEIRGKTLGI IGYGHIGSQL SVLAEAMGLH VVYYDILPIM PLGSAKQLSS 

       250        260        270        280        290        300 
LPELLHRADF VSLHVPASPE TKNMISSKEF AAMKEGSYLI NASRGTVVDI PALVDASKSG 

       310        320        330        340        350        360 
KIAGAAIDVY PSEPAGNGKD KFVDSLNSWT SELTHCKNII LTPHIGGSTE EAQYNIGIEV 

       370        380        390        400        410        420 
SEALTRYINE GNSIGAVNFP EVSLRSLTEA DRNAARVLFV HRNVPGVLRQ VNELFIDHNI 

       430        440        450        460 
KSQFSDSRGD IAYLVADISD CTPGSLEALH QKLESLPCKI NTRLLY 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-258, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAB09778.1.
PIRT41375.
RefSeqNP_587837.1. NM_001022830.1.

3D structure databases

ProteinModelPortalP87228.
ModBaseSearch...

Protein-protein interaction databases

STRINGP87228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC364.07.1; SPCC364.07.1:pep; SPCC364.07.
GeneID2539490.
KEGGspo:SPCC364.07.
NMPDRfig|4896.1.peg.175.

Organism-specific databases

GeneDB_SpombeSPCC364.07.

Phylogenomic databases

eggNOGfuNOG05789.
GeneTreeEFGT00050000001276.
HOGENOMHBG731446.
OMARGGWLKS.
OrthoDBEOG4NGKWJ.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002412-MONOMER.

Gene expression databases

ArrayExpressP87228.

Family and domain databases

InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KOK00058.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERA_SCHPO
AccessionPrimary (citable) accession number: P87228
Secondary accession number(s): O59798
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families